Related Experiment Video
Updated: Nov 27, 2025

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
Structure of the activated ROQ1 resistosome directly recognizing the pathogen effector XopQ
Raoul Martin1,2, Tiancong Qi3,4, Haibo Zhang3
1Biophysics Graduate Group, University of California, Berkeley, CA 94720, USA.
None:
Plants and animals detect pathogen infection using intracellular nucleotide-binding leucine-rich repeat receptors (NLRs) that directly or indirectly recognize pathogen effectors and activate an immune response. How effector sensing triggers NLR activation remains poorly understood. Here we describe the 3.8-angstrom-resolution cryo-electron microscopy structure of the activated ROQ1 (recognition of XopQ 1), an NLR native to Nicotiana benthamiana with a Toll-like interleukin-1 receptor (TIR) domain bound to the Xanthomonas euvesicatoria effector XopQ (Xanthomonas outer protein Q). ROQ1 directly binds to both the predicted active site and surface residues of XopQ while forming a tetrameric resistosome that brings together the TIR domains for downstream immune signaling. Our results suggest a mechanism for the direct recognition of effectors by NLRs leading to the oligomerization-dependent activation of a plant resistosome and signaling by the TIR domain.
Related Concept Videos
Regulation of the Unfolded Protein Response
Gene Regulation in Microbial Communities: Quorum Sensing
Global Regulatory Systems
Antigen Processing Pathways
MHC Class I: Presenting Endogenous...
Exon Recombination
Exon shuffling follows “splice frame rules.” Each exon...
Protein Import into the Peroxisomes
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...

